Evidence map›Paper›PMID 30611424›Full record

ArticleMethods in enzymology2019

Preparation of Phosphorylated Proteins for NMR Spectroscopy.

Ganesan Senthil Kumar, Rebecca Page, Wolfgang Peti

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Methods in enzymology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

3 citing papers in PubMed.

  1. Tyrosine kinases sample unique activation ensembles.bioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. International journal of molecular sciences · 2019
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Ganesan Senthil KumarDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, AZ, United States.
Rebecca PageDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, AZ, United States.
Wolfgang PetiDepartment of Chemistry and Biochemistry, University of Arizona, Tucson, AZ, United States. Electronic address: wolfgangpeti@email.arizona.edu.

Funding

The Regulation of PP1 in the NucleusR01GM098482 · NIGMS · UNIVERSITY OF ARIZONA · PI PAGE, REBECCA · 2011 to 2019
$2.8M
Supplement for "Serine/Threonine Phosphatases in Neurological Diseases"R01NS091336 · NINDS · UNIVERSITY OF ARIZONA · PI PAGE, REBECCA, PETI, WOLFGANG · 2015 to 2019
$1.8M
Dynamics & energetics of p38a kinase regulation by ligandsR01GM100910 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI PETI, WOLFGANG, WAND, A. JOSHUA · 2013 to 2016
$1.3M
Protein Phosphatase 1 Holoenzyme Formation and Subunit ExchangeR01GM134683 · NIGMS · UNIVERSITY OF ARIZONA · PI PETI, WOLFGANG · 2019 to 2020
$564k
NIGMS NIH HHS R01 GM098482NIGMS NIH HHS R01 GM100910NIGMS NIH HHS R01 GM134683NINDS NIH HHS R01 NS091336
6 · The paper itself

Abstract

Phosphorylation is a ubiquitous posttranslational modification that is essential for the regulation of many cellular processes. The human genome consists of more than 200,000 phosphorylation sites, whose phosphorylation is tightly controlled by ≥500 kinases and ~200 phosphatases. Given the large number of phosphorylation sites and the key role phosphorylation plays in regulating cellular processes, it is essential to characterize the impact of phosphorylation on substrate structure, dynamics, and function. However, a major challenge is the large-scale production of phosphorylated proteins in vitro for these structural, functional, and dynamic studies. Here, we describe an efficient protocol used routinely in our laboratory for the production of phosphorylated proteins. We also describe the methods used for identifying, characterizing, and separating the resulting phosphorylated proteins for subsequent studies.

Indexed as

Protein Processing, Post-TranslationalAdenosine TriphosphateElectrophoresis, Polyacrylamide GelHumansKi-67 AntigenMAP Kinase Kinase 6Nuclear Magnetic Resonance, Biomolecularp38 Mitogen-Activated Protein KinasesPhosphorylationSubstrate SpecificityAdenosine TriphosphateKi-67 AntigenMAP2K6 protein, humanMAP Kinase Kinase 6p38 Mitogen-Activated Protein KinasesKinaseNMR spectroscopyPhosphatasePhosphorylationPosttranslational modificationProtein expression

Identifiers

PMID30611424
PMCPMC13007556

What OpenQuestion holds

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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.